KMT5A explained
N-lysine methyltransferase KMT5A is an enzyme that in humans is encoded by the KMT5A gene.[1] [2] [3] [4] The enzyme is a histone methyltransferase, SET domain-containing and lysine-specific. The enzyme transfers one methyl group to histone H4 lysine residue at position 20. S-Adenosyl methionine (SAM) is both the cofactor and the methyl group donor. The lysine residue is converted to N6-methyllysine residue.
This histone modification is often abbreviated H4K20me1:
- H4 - type of histone
- K - symbol of lysine
- 20 - position of the lysine residue modified
- me - abbreviation for methyl group
- 1 - number of methyl groups transferred
Further reading
- Mizzen CA, Yang XJ, Kokubo T, Brownell JE, Bannister AJ, Owen-Hughes T, Workman J, Wang L, Berger SL, Kouzarides T, Nakatani Y, Allis CD . The TAF(II)250 subunit of TFIID has histone acetyltransferase activity . Cell . 87 . 7 . 1261–70 . December 1996 . 8980232 . 10.1016/S0092-8674(00)81821-8 . 18409257 . free .
- Rice JC, Nishioka K, Sarma K, Steward R, Reinberg D, Allis CD . Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes . Genes & Development . 16 . 17 . 2225–30 . September 2002 . 12208845 . 186671 . 10.1101/gad.1014902 .
- Schlisio S, Halperin T, Vidal M, Nevins JR . Interaction of YY1 with E2Fs, mediated by RYBP, provides a mechanism for specificity of E2F function . The EMBO Journal . 21 . 21 . 5775–86 . November 2002 . 12411495 . 131074 . 10.1093/emboj/cdf577 .
- Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ . Structure and catalytic mechanism of the human histone methyltransferase SET7/9 . Nature . 421 . 6923 . 652–6 . February 2003 . 12540855 . 10.1038/nature01378 . 2003Natur.421..652X . 4423407 .
- Xiao B, Jing C, Kelly G, Walker PA, Muskett FW, Frenkiel TA, Martin SR, Sarma K, Reinberg D, Gamblin SJ, Wilson JR . Specificity and mechanism of the histone methyltransferase Pr-Set7 . Genes & Development . 19 . 12 . 1444–54 . June 2005 . 15933069 . 1151661 . 10.1101/gad.1315905 .
- Yin Y, Liu C, Tsai SN, Zhou B, Ngai SM, Zhu G . SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20 . The Journal of Biological Chemistry . 280 . 34 . 30025–31 . August 2005 . 15964846 . 10.1074/jbc.M501691200 . free .
- Shi X, Kachirskaia I, Yamaguchi H, West LE, Wen H, Wang EW, Dutta S, Appella E, Gozani O . Modulation of p53 function by SET8-mediated methylation at lysine 382 . Molecular Cell . 27 . 4 . 636–46 . August 2007 . 17707234 . 2693209 . 10.1016/j.molcel.2007.07.012 .
- Tanaka H, Takebayashi SI, Sakamoto A, Igata T, Nakatsu Y, Saitoh N, Hino S, Nakao M . The SETD8/PR-Set7 Methyltransferase Functions as a Barrier to Prevent Senescence-Associated Metabolic Remodeling . Cell Reports . 18 . 9 . 2148–2161 . February 2017 . 28249161. 10.1016/j.celrep.2017.02.021 . free .
Notes and References
- Couture JF, Collazo E, Brunzelle JS, Trievel RC . Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase . Genes & Development . 19 . 12 . 1455–65 . June 2005 . 15933070 . 1151662 . 10.1101/gad.1318405 .
- Nishioka K, Rice JC, Sarma K, Erdjument-Bromage H, Werner J, Wang Y, Chuikov S, Valenzuela P, Tempst P, Steward R, Lis JT, Allis CD, Reinberg D . PR-Set7 is a nucleosome-specific methyltransferase that modifies lysine 20 of histone H4 and is associated with silent chromatin . Molecular Cell . 9 . 6 . 1201–13 . June 2002 . 12086618 . 10.1016/S1097-2765(02)00548-8 . free .
- Fang J, Feng Q, Ketel CS, Wang H, Cao R, Xia L, Erdjument-Bromage H, Tempst P, Simon JA, Zhang Y . Purification and functional characterization of SET8, a nucleosomal histone H4-lysine 20-specific methyltransferase . Current Biology . 12 . 13 . 1086–99 . July 2002 . 12121615 . 10.1016/S0960-9822(02)00924-7 . 15504308 . free . 2002CBio...12.1086F .
- Web site: Entrez Gene: KMT5A lysine methyltransferase 5A [Homo sapiens (human) ]].